메뉴 건너뛰기




Volumn 92, Issue 2, 2004, Pages 288-297

Aberrant mucosal wound repair in the absence of secretory leukocyte protease inhibitor

Author keywords

Cutaneous; Inflammation; Mucosa; Oral; SLPI; Wound healing

Indexed keywords

COLLAGEN; ELASTASE; MATRIX METALLOPROTEINASE; SECRETORY LEUKOCYTE PROTEINASE INHIBITOR; TRANSFORMING GROWTH FACTOR BETA;

EID: 4444350478     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/th03-07-0446     Document Type: Article
Times cited : (61)

References (49)
  • 1
    • 0024498944 scopus 로고
    • Tissue distribution of antileukoprotease and lysozyme in humans
    • Franken C, Meijer CJ, Dijkman JH. Tissue distribution of antileukoprotease and lysozyme in humans. J Histochem Cytochem 1989; 37(4): 493-8.
    • (1989) J. Histochem. Cytochem. , vol.37 , Issue.4 , pp. 493-498
    • Franken, C.1    Meijer, C.J.2    Dijkman, J.H.3
  • 2
    • 0036545373 scopus 로고    scopus 로고
    • Novel roles of protease inhibitors in infection and inflammation
    • Hiemstra PS. Novel roles of protease inhibitors in infection and inflammation. Biochem Soc Trans 2002; 30(2): 116-20.
    • (2002) Biochem. Soc. Trans. , vol.30 , Issue.2 , pp. 116-120
    • Hiemstra, P.S.1
  • 3
    • 0033787069 scopus 로고    scopus 로고
    • Secretory leukocyte protease inhibitor mediates nonredundant functions necessary for normal wound healing
    • Ashcroft GS, Lei K, Jin W, et al.. Secretory leukocyte protease inhibitor mediates nonredundant functions necessary for normal wound healing. Nat Med 2000; 6(10): 1147-53.
    • (2000) Nat. Med. , vol.6 , Issue.10 , pp. 1147-1153
    • Ashcroft, G.S.1    Lei, K.2    Jin, W.3
  • 4
    • 0030941175 scopus 로고    scopus 로고
    • Secretory leukocyte protease inhibitor: A macrophage product induced by and antagonistic to bacterial lipopolysaccharide
    • Jin FY, Nathan C, Radzioch D, et al.. Secretory leukocyte protease inhibitor: a macrophage product induced by and antagonistic to bacterial lipopolysaccharide. Cell 1997; 88(3): 417-26.
    • (1997) Cell , vol.88 , Issue.3 , pp. 417-426
    • Jin, F.Y.1    Nathan, C.2    Radzioch, D.3
  • 5
    • 0033575758 scopus 로고    scopus 로고
    • Secretory leukocyte protease inhibitor suppresses the inflammation and joint damage of bacterial cell wall-induced arthritis
    • Song X, Zeng L, Jin W, et al.. Secretory leukocyte protease inhibitor suppresses the inflammation and joint damage of bacterial cell wall-induced arthritis. J Exp Med 1999; 190(4): 535-42.
    • (1999) J. Exp. Med. , vol.190 , Issue.4 , pp. 535-542
    • Song, X.1    Zeng, L.2    Jin, W.3
  • 6
    • 0037074016 scopus 로고    scopus 로고
    • Conversion of proepithelin to epithelins: Roles of SLPI and elastase in host defense and wound repair
    • Zhu J, Nathan C, Jin W, et al.. Conversion of proepithelin to epithelins: roles of SLPI and elastase in host defense and wound repair. Cell 2002; 111(6): 867-78.
    • (2002) Cell , vol.111 , Issue.6 , pp. 867-878
    • Zhu, J.1    Nathan, C.2    Jin, W.3
  • 7
    • 0012030796 scopus 로고
    • Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor, a potent inhibitor of leukocyte elastase
    • Thompson RC, Ohlsson K. Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor, a potent inhibitor of leukocyte elastase. Proc Natl Acad Sci U S A 1986; 83(18): 6692-6.
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , Issue.18 , pp. 6692-6696
    • Thompson, R.C.1    Ohlsson, K.2
  • 8
    • 0036547750 scopus 로고    scopus 로고
    • Antimicrobial activity of antiproteinases
    • Sallenave JM. Antimicrobial activity of antiproteinases. Biochem Soc Trans 2002; 30(2): 111-5.
    • (2002) Biochem. Soc. Trans. , vol.30 , Issue.2 , pp. 111-115
    • Sallenave, J.M.1
  • 9
    • 0032112238 scopus 로고    scopus 로고
    • The role of the oral environment in HIV-1 transmission
    • Shugars DC, Wahl SM. The role of the oral environment in HIV-1 transmission. J Am Dent Assoc 1998; 129(7): 851-8.
    • (1998) J. Am. Dent. Assoc. , vol.129 , Issue.7 , pp. 851-858
    • Shugars, D.C.1    Wahl, S.M.2
  • 10
    • 0030741731 scopus 로고    scopus 로고
    • Inhibition of human immunodeficiency virus type 1 infectivity by secretory leukocyte protease inhibitor occurs prior to viral reverse transcription
    • McNeely TB, Shugars DC, Rosendahl M, et al. Inhibition of human immunodeficiency virus type 1 infectivity by secretory leukocyte protease inhibitor occurs prior to viral reverse transcription. Blood 1997; 90(3): 1141-9.
    • (1997) Blood , vol.90 , Issue.3 , pp. 1141-1149
    • McNeely, T.B.1    Shugars, D.C.2    Rosendahl, M.3
  • 11
    • 0029115952 scopus 로고
    • Secretory leukocyte protease inhibitor: A human saliva protein exhibiting anti-human immunodeficiency virus 1 activity in vitro
    • McNeely TB, Dealy M, Dripps DJ, et al.. Secretory leukocyte protease inhibitor: a human saliva protein exhibiting anti-human immunodeficiency virus 1 activity in vitro. J Clin Invest 1995; 96(1): 456-64.
    • (1995) J. Clin. Invest. , vol.96 , Issue.1 , pp. 456-464
    • McNeely, T.B.1    Dealy, M.2    Dripps, D.J.3
  • 12
    • 4243600234 scopus 로고    scopus 로고
    • Endogenous regulation of the acute inflammatory response
    • Ward PA, Lentsch AB. Endogenous regulation of the acute inflammatory response. Mol Cell Biochem 2002; 234-235(1-2): 225-8.
    • (2002) Mol. Cell Biochem. , vol.234-235 , Issue.1-2 , pp. 225-228
    • Ward, P.A.1    Lentsch, A.B.2
  • 13
    • 0019200629 scopus 로고
    • Degradation of fibronectin by human leukocyte elastase. Release of biologically active fragments
    • McDonald JA, Kelley DG. Degradation of fibronectin by human leukocyte elastase. Release of biologically active fragments. J Biol Chem 1980; 255(18): 8848-58.
    • (1980) J. Biol. Chem. , vol.255 , Issue.18 , pp. 8848-8858
    • McDonald, J.A.1    Kelley, D.G.2
  • 14
    • 0025732513 scopus 로고
    • Cathepsin-G and leukocyte elastase inactivate human tumor necrosis factor and lymphotoxin
    • Scuderi P, Nez PA, Duerr ML, et al.. Cathepsin-G and leukocyte elastase inactivate human tumor necrosis factor and lymphotoxin. Cell Immunol 1991; 135(2): 299-313.
    • (1991) Cell Immunol. , vol.135 , Issue.2 , pp. 299-313
    • Scuderi, P.1    Nez, P.A.2    Duerr, M.L.3
  • 15
    • 0032030785 scopus 로고    scopus 로고
    • Cleavage of native type I collagen by human neutrophil elastase
    • Kafienah W, Buttle DJ, Burnett D, et al.. Cleavage of native type I collagen by human neutrophil elastase. Biochem J 1998; 330 (Pt 2): 897-902.
    • (1998) Biochem. J. , vol.330 , Issue.PART 2 , pp. 897-902
    • Kafienah, W.1    Buttle, D.J.2    Burnett, D.3
  • 16
    • 0030307261 scopus 로고    scopus 로고
    • A comparison of the ability of intra-oral and extra-oral fibroblasts to stimulate extracellular matrix reorganization in a model of wound contraction
    • Stephens P, Davies KJ, al-Khateeb T, et al.. A comparison of the ability of intra-oral and extra-oral fibroblasts to stimulate extracellular matrix reorganization in a model of wound contraction. J Dent Res 1996; 75(6): 1358-64.
    • (1996) J. Dent. Res. , vol.75 , Issue.6 , pp. 1358-1364
    • Stephens, P.1    Davies, K.J.2    al-Khateeb, T.3
  • 18
    • 0038748039 scopus 로고    scopus 로고
    • The effect of combined rapamycin/cyclosporine on the changes in pro-fibrotic gene expression that occur during the development of allograft vasculopathy in rats, compared with cyclosporine or rapamycin in isolation
    • Murphy GJ, Bicknell GR, Nicholson ML. The effect of combined rapamycin/cyclosporine on the changes in pro-fibrotic gene expression that occur during the development of allograft vasculopathy in rats, compared with cyclosporine or rapamycin in isolation. Transpl Int 2003; 16(5): 347-53.
    • (2003) Transpl. Int. , vol.16 , Issue.5 , pp. 347-353
    • Murphy, G.J.1    Bicknell, G.R.2    Nicholson, M.L.3
  • 19
    • 0027169767 scopus 로고
    • A reagent for the single-step simultaneous isolation of RNA, DNA and proteins from cell and tissue samples
    • 532-4
    • Chomczynski P. A reagent for the single-step simultaneous isolation of RNA, DNA and proteins from cell and tissue samples. Biotechniques 1993; 15(3): 532-4, 536-7.
    • (1993) Biotechniques , vol.15 , Issue.3 , pp. 536-537
    • Chomczynski, P.1
  • 20
    • 0035710229 scopus 로고    scopus 로고
    • An overview of real-time quantitative PCR: Applications to quantify cytokine gene expression
    • Giulietti A, Overbergh L, Valckx D, et al.. An overview of real-time quantitative PCR: applications to quantify cytokine gene expression. Methods 2001; 25(4): 386-401.
    • (2001) Methods , vol.25 , Issue.4 , pp. 386-401
    • Giulietti, A.1    Overbergh, L.2    Valckx, D.3
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72: 248-54.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 0032510164 scopus 로고    scopus 로고
    • Ursolic acid-induced down-regulation of MMP-9 gene is mediated through the nuclear translocation of glucocorticoid receptor in HT1080 human fibrosarcoma cells
    • Cha HJ, Park MT, Chung HY, et al.. Ursolic acid-induced down-regulation of MMP-9 gene is mediated through the nuclear translocation of glucocorticoid receptor in HT1080 human fibrosarcoma cells. Oncogene 1998; 16(6): 771-8.
    • (1998) Oncogene , vol.16 , Issue.6 , pp. 771-778
    • Cha, H.J.1    Park, M.T.2    Chung, H.Y.3
  • 23
    • 0024330327 scopus 로고
    • SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages
    • Wilhelm SM, Collier IE, Marmer BL, et al.. SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages. J Biol Chem 1989; 264(29): 17213-21
    • (1989) J. Biol. Chem. , vol.264 , Issue.29 , pp. 17213-17221
    • Wilhelm, S.M.1    Collier, I.E.2    Marmer, B.L.3
  • 24
    • 0035156633 scopus 로고    scopus 로고
    • TNF-alpha stimulates activation of pro-MMP2 in human skin through NF-(kappa)B mediated induction of MT1-MMP
    • Han YP, Tuan TL, Wu H, et al.. TNF-alpha stimulates activation of pro-MMP2 in human skin through NF-(kappa)B mediated induction of MT1-MMP. J Cell Sci 2001; 114 (Pt 1): 131-9.
    • (2001) J. Cell Sci. , vol.114 , Issue.PART 1 , pp. 131-139
    • Han, Y.P.1    Tuan, T.L.2    Wu, H.3
  • 25
    • 0032870946 scopus 로고    scopus 로고
    • Topical estrogen accelerates cutaneous wound healing in aged humans associated with an altered inflammatory response
    • Ashcroft GS, Greenwell-Wild T, Horan MA, et al.. Topical estrogen accelerates cutaneous wound healing in aged humans associated with an altered inflammatory response. Am J Pathol 1999; 155(4): 1137-46.
    • (1999) Am. J. Pathol. , vol.155 , Issue.4 , pp. 1137-1146
    • Ashcroft, G.S.1    Greenwell-Wild, T.2    Horan, M.A.3
  • 26
    • 0030880539 scopus 로고    scopus 로고
    • Upregulation of elastase in acute wounds of healthy aged humans and chronic venous leg ulcers are associated with matrix degradation
    • Herrick S, Ashcroft G, Ireland G, et al.. Upregulation of elastase in acute wounds of healthy aged humans and chronic venous leg ulcers are associated with matrix degradation. Lab Invest 1997; 77(3): 281-8.
    • (1997) Lab. Invest. , vol.77 , Issue.3 , pp. 281-288
    • Herrick, S.1    Ashcroft, G.2    Ireland, G.3
  • 28
    • 0033517356 scopus 로고    scopus 로고
    • Cutaneous wound healing
    • Singer AJ, Clark RA. Cutaneous wound healing. N Engl J Med 1999; 341(10): 738-46.
    • (1999) N. Engl. J. Med. , vol.341 , Issue.10 , pp. 738-746
    • Singer, A.J.1    Clark, R.A.2
  • 29
    • 2342496439 scopus 로고
    • Transforming growth factor type beta induces monocyte chemotaxis and growth factor production
    • Wahl SM, Hunt DA, Wakefield LM, et al.. Transforming growth factor type beta induces monocyte chemotaxis and growth factor production. Proc Natl Acad Sci U S A 1987; 84(16): 5788-92.
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , Issue.16 , pp. 5788-5792
    • Wahl, S.M.1    Hunt, D.A.2    Wakefield, L.M.3
  • 30
    • 0029875396 scopus 로고    scopus 로고
    • Transforming growth factors beta1, beta2, and beta3 and their receptors are differentially regulated during normal and impaired wound healing
    • Frank S, Madlener M, Werner S. Transforming growth factors beta1, beta2, and beta3 and their receptors are differentially regulated during normal and impaired wound healing. J Biol Chem 1996; 271(17): 10188-93.
    • (1996) J. Biol. Chem. , vol.271 , Issue.17 , pp. 10188-10193
    • Frank, S.1    Madlener, M.2    Werner, S.3
  • 32
    • 0037295872 scopus 로고    scopus 로고
    • Healing is delayed in oral compared to dermal excisional wounds
    • Nooh N, Graves DT. Healing is delayed in oral compared to dermal excisional wounds. J Periodontol 2003; 74(2): 242-6.
    • (2003) J. Periodontol. , vol.74 , Issue.2 , pp. 242-246
    • Nooh, N.1    Graves, D.T.2
  • 33
    • 0035461854 scopus 로고    scopus 로고
    • Reduced oral wound healing in the NOD mouse model for type 1 autoinumme diabetes and its reversal by epidermal growth factor supplementation
    • Nagy A, Nagashima H, Cha S, et al.. Reduced oral wound healing in the NOD mouse model for type 1 autoinumme diabetes and its reversal by epidermal growth factor supplementation. Diabetes 2001; 50(9): 2100-4.
    • (2001) Diabetes , vol.50 , Issue.9 , pp. 2100-2104
    • Nagy, A.1    Nagashima, H.2    Cha, S.3
  • 34
    • 0036893380 scopus 로고    scopus 로고
    • Antimicrobial agents in saliva-protection for the whole body
    • Tenovuo J. Antimicrobial agents in saliva-protection for the whole body. J Dent Res 2002; 81(12): 807-9.
    • (2002) J. Dent. Res. , vol.81 , Issue.12 , pp. 807-809
    • Tenovuo, J.1
  • 35
    • 0038726949 scopus 로고    scopus 로고
    • Different mechanisms of syndecan-1 activation through a fibroblast-growth-factor-inducible response element (FiRE) in mucosal and cutaneous wounds
    • Rautava J, Soukka T, Heikinheimo K, et al.. Different mechanisms of syndecan-1 activation through a fibroblast-growth-factor-inducible response element (FiRE) in mucosal and cutaneous wounds. J Dent Res 2003; 82(5): 382-7.
    • (2003) J. Dent. Res. , vol.82 , Issue.5 , pp. 382-387
    • Rautava, J.1    Soukka, T.2    Heikinheimo, K.3
  • 36
    • 0026149768 scopus 로고
    • Current concepts of the role of fibroblasts and extracellular matrix in wound healing and their relevance to oral implantology
    • Sloan P. Current concepts of the role of fibroblasts and extracellular matrix in wound healing and their relevance to oral implantology. J Dent 1991; 19(2): 107-9.
    • (1991) J. Dent. , vol.19 , Issue.2 , pp. 107-109
    • Sloan, P.1
  • 37
    • 0028229804 scopus 로고
    • Inter- and intra-site heterogeneity in the expression of fetal-like phenotypic characteristics by gingival fibroblasts: Potential significance for wound healing
    • Irwin CR, Picardo M, Ellis I, et al.. Inter- and intra-site heterogeneity in the expression of fetal-like phenotypic characteristics by gingival fibroblasts: potential significance for wound healing. J Cell Sci 1994; 107 (Pt 5): 1333-46.
    • (1994) J. Cell Sci. , vol.107 , Issue.PART 5 , pp. 1333-1346
    • Irwin, C.R.1    Picardo, M.2    Ellis, I.3
  • 38
    • 0031262410 scopus 로고    scopus 로고
    • An investigation of preferential fibroblast wound repopulation using a novel in vitro wound model
    • al-Khateeb T, Stephens P, Shepherd JP, et al.. An investigation of preferential fibroblast wound repopulation using a novel in vitro wound model. J Periodontol 1997; 68(11): 1063-9.
    • (1997) J. Periodontol. , vol.68 , Issue.11 , pp. 1063-1069
    • al-Khateeb, T.1    Stephens, P.2    Shepherd, J.P.3
  • 39
    • 0032845744 scopus 로고    scopus 로고
    • Differences between fibroblasts cultured from oral mucosa and normal skin: Implication to wound healing
    • Lee HG, Eun HC. Differences between fibroblasts cultured from oral mucosa and normal skin: implication to wound healing. J Dermatol Sci 1999; 21(3): 176-82.
    • (1999) J. Dermatol. Sci. , vol.21 , Issue.3 , pp. 176-182
    • Lee, H.G.1    Eun, H.C.2
  • 40
    • 0035500631 scopus 로고    scopus 로고
    • IL-1 plays a critical role in oral, but not dermal, wound healing
    • Graves DT, Nooh N, Gillen T, et al.. IL-1 plays a critical role in oral, but not dermal, wound healing. J Immunol 2001; 167(9): 5316-20.
    • (2001) J. Immunol. , vol.167 , Issue.9 , pp. 5316-5320
    • Graves, D.T.1    Nooh, N.2    Gillen, T.3
  • 41
    • 13344262698 scopus 로고    scopus 로고
    • Salivary EGF regulates eosinophil-derived TGF-alpha expression in hamster oral wounds
    • Yang J, Tyler LW, Donoff RB, et al.. Salivary EGF regulates eosinophil-derived TGF-alpha expression in hamster oral wounds. Am J Physiol 1996; 270(1 Pt 1): G191-202.
    • (1996) Am. J. Physiol. , vol.270 , Issue.1 PART 1
    • Yang, J.1    Tyler, L.W.2    Donoff, R.B.3
  • 42
    • 0030786999 scopus 로고    scopus 로고
    • Transforming growth factor beta 1 and its latent form binding protein-1 associate with elastic fibres in human dermis: Accumulation in actinic damage and absence in anetoderma
    • Karonen T, Jeskanen L, Keski-Oja J. Transforming growth factor beta 1 and its latent form binding protein-1 associate with elastic fibres in human dermis: accumulation in actinic damage and absence in anetoderma. Br J Dermatol 1997; 137(1): 51-8.
    • (1997) Br. J. Dermatol. , vol.137 , Issue.1 , pp. 51-58
    • Karonen, T.1    Jeskanen, L.2    Keski-Oja, J.3
  • 43
    • 0028956737 scopus 로고
    • Human mast cell chymase and leukocyte elastase release latent transforming growth factor-beta 1 from the extracellular matrix of cultured human epithelial and endothelial cells
    • Taipale J, Lohi J, Saarinen J, et al.. Human mast cell chymase and leukocyte elastase release latent transforming growth factor-beta 1 from the extracellular matrix of cultured human epithelial and endothelial cells. J Biol Chem 1995; 270(9): 4689-96.
    • (1995) J. Biol. Chem. , vol.270 , Issue.9 , pp. 4689-4696
    • Taipale, J.1    Lohi, J.2    Saarinen, J.3
  • 44
    • 0027283014 scopus 로고
    • PGAIPG, a repeated hexapeptide of bovine and human tropoelastin, is chemotactic for neutrophils and Lewis lung carcinoma cells
    • Grosso LE, Scott M. PGAIPG, a repeated hexapeptide of bovine and human tropoelastin, is chemotactic for neutrophils and Lewis lung carcinoma cells. Arch Biochem Biophys 1993; 305(2): 401-4.
    • (1993) Arch. Biochem. Biophys. , vol.305 , Issue.2 , pp. 401-404
    • Grosso, L.E.1    Scott, M.2
  • 45
    • 0025946070 scopus 로고
    • Immunohistochemical localization of growth factors in fetal wound healing
    • Whitby DJ, Ferguson MW. Immunohistochemical localization of growth factors in fetal wound healing. Dev Biol 1991; 147(1): 207-15.
    • (1991) Dev. Biol. , vol.147 , Issue.1 , pp. 207-215
    • Whitby, D.J.1    Ferguson, M.W.2
  • 46
    • 0028219896 scopus 로고
    • The expression of transforming growth factor type beta in fetal and adult rabbit skin wounds
    • Nath RK, LaRegina M, Markham H, et al.. The expression of transforming growth factor type beta in fetal and adult rabbit skin wounds. J Pediatr Surg 1994; 29(3): 416-21.
    • (1994) J. Pediatr. Surg. , vol.29 , Issue.3 , pp. 416-421
    • Nath, R.K.1    LaRegina, M.2    Markham, H.3
  • 47
    • 0028893942 scopus 로고
    • A model of scarless human fetal wound repair is deficient in transforming growth factor beta
    • discussion 202-3
    • Sullivan KM, Lorenz HP, Meuli M, et al.. A model of scarless human fetal wound repair is deficient in transforming growth factor beta. J Pediatr Surg 1995; 30(2): 198-202; discussion 202-3.
    • (1995) J. Pediatr. Surg. , vol.30 , Issue.2 , pp. 198-202
    • Sullivan, K.M.1    Lorenz, H.P.2    Meuli, M.3
  • 48
    • 0026505458 scopus 로고
    • Control of scarring in adult wounds by neutralising antibody to transforming growth factor beta
    • Shah M, Foreman DM, Ferguson MW. Control of scarring in adult wounds by neutralising antibody to transforming growth factor beta. Lancet 1992; 339(8787): 213-4.
    • (1992) Lancet , vol.339 , Issue.8787 , pp. 213-214
    • Shah, M.1    Foreman, D.M.2    Ferguson, M.W.3
  • 49
    • 0033195998 scopus 로고    scopus 로고
    • Mice lacking Smad3 show accelerated wound healing and an impaired local inflammatory response
    • Ashcroft GS, Yang X, Glick AB, et al.. Mice lacking Smad3 show accelerated wound healing and an impaired local inflammatory response. Nat Cell Biol 1999; 1(5): 260-6.
    • (1999) Nat. Cell Biol. , vol.1 , Issue.5 , pp. 260-266
    • Ashcroft, G.S.1    Yang, X.2    Glick, A.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.